1.4.3.5	pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2	enzyme is not stereospecific and catalyzes removal of either pro-R or pro-S hydrogen from 4-methylene of pyridoxamine 5' phosphate	391872	
1.4.3.5	pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2	enzyme is specific for removal of the pro-R hydrogen atom from the prochiral C4' carbon atom of pyridoxamine 5'-phosphate, hydride ion mechanism is suggested	391906	
1.4.3.5	pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2	kinetic mechanims via either a binary or a ternary complex mechanism, depending on nature of substrate, ternary complex mechanism with pyridoxamine 5'-phosphate	391878	
1.4.3.5	pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2	reaction mechanism	391890	
1.4.3.5	pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2	reaction mechanism, the oxidation involves a stereospecific hydride-ion transfer between C4' of pyridoxal 5'-phosphate and N5 of FMN, structure-function relationship, substrate binding and active site structure	667050	
1.4.3.5	pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2	-	-	
1.4.3.5	pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2	reaction mechanism	391890	
1.4.3.5	pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2	reaction mechanism, the oxidation involves a stereospecific hydride-ion transfer between C4' of pyridoxal 5'-phosphate and N5 of FMN, structure-function relationship, substrate binding and active site structure	667050